Durban E, Valdez B C, Gustafson W C, Taylor C W, Cardellini E, Busch H
Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030, USA.
Physiol Chem Phys Med NMR. 1995;27(4):303-11.
Nucleolar phosphoprotein p120 is a low abundance, proliferation-associated protein. Several functional domains have been characterized and are discussed here such as the antigenic domain recognized by a monoclonal antibody, the nuclear/nucleolar localization domain, phosphorylation domains of casein kinase II (CKII) and protein kinase C, a putative methylation domain and an RNA binding region. By sucrose gradient sedimentation analyses, protein p120 was shown to rapidly sediment with 60-80 S pre-rRNP particles but sedimented more slowly when treated with RNAse or salt suggesting binding to RNA. Nucleolar protein p120 differed from other nucleolar proteins such as C23 (nucleolin) and B23 (nucleophosmin) which sedimented more slowly near the top of the gradient.
核仁磷蛋白p120是一种低丰度的、与增殖相关的蛋白质。已对几个功能结构域进行了表征并在此进行讨论，例如单克隆抗体识别的抗原结构域、核/核仁定位结构域、酪蛋白激酶II（CKII）和蛋白激酶C的磷酸化结构域、一个假定的甲基化结构域以及一个RNA结合区域。通过蔗糖梯度沉降分析表明，蛋白p120能与60 - 80 S前体核糖体核糖核蛋白（pre - rRNP）颗粒快速沉降，但在用核糖核酸酶或盐处理时沉降较慢，这表明它与RNA结合。核仁蛋白p120与其他核仁蛋白不同，如C23（核仁素）和B23（核磷蛋白），它们在梯度顶部附近沉降较慢。
